Anion binding to hydrophobic concavity is central to the salting-in effects of Hofmeister chaotropes.
Anion binding to hydrophobic concavity is central to the salting-in effects of Hofmeister chaotropes.
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DOI：
10.1021/ja202308n
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发表时间：
2011-05-18
影响因子：
15
通讯作者：
Gibb, Bruce C.
中科院分区：
文献类型：
--
作者：
Gibb, Corinne L. D.;Gibb, Bruce C.
120多年来，人们已经认识到，某些盐（kosmotropes）会导致蛋白质沉淀，而其他盐（离液剂）会增加蛋白质的溶解度。其原因，“霍夫迈斯特效应”仍然不清楚;特别是与最初的概念，即亲液阴离子“制造”水结构和离液剂“破坏”它被最近的研究提出相反的建议。在这里，我们提出了第一个直接的证据，即离液阴离子具有亲合力的疏水疏水性，它是一个凸的疏水和阴离子之间的竞争，导致明显减弱的疏水效果的结合位点的离液剂。总之，这些结果表明，离液剂主要通过直接结合到蛋白质的熔融球状态的β-淀粉酶来诱导蛋白质溶解。
For over 120 years it has been appreciated that certain salts (kosmotropes) cause the precipitation of proteins, whilst others (chaotropes) increase their solubility. The cause of this, “Hofmeister effect” is still unclear; especially with the original concept that kosmotropic anions “make” water structure and chaotropes “break” it being countered by recent studies suggesting otherwise. Here, we present the first direct evidence that chaotropic anions have an affinity for hydrophobic concavity, and that it is competition between a convex hydrophobe and the anion for a binding site that leads to the apparent weakening of the hydrophobic effect by chaotropes. In combination, these results suggest that chaotropes primarily induce protein solubilization by direct binding to concavity in the molten globule state of a protein.
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影响因子：
3.3
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Sun, Hao;Gibb, Corinne L. D.;Gibb, Bruce C.
通讯作者：
Gibb, Bruce C.
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